ID   GL117_ARATH             Reviewed;         221 AA.
AC   Q9FIC6;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Germin-like protein subfamily 1 member 17;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g39150; ORFNames=MXF12.18, MXF12_160;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
CC   -!- FUNCTION: May play a role in plant defense. Probably has no oxalate
CC       oxidase activity even if the active site is conserved.
CC   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; AB016892; BAB10836.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94399.1; -; Genomic_DNA.
DR   EMBL; BX833065; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_198731.1; NM_123277.4.
DR   AlphaFoldDB; Q9FIC6; -.
DR   SMR; Q9FIC6; -.
DR   STRING; 3702.AT5G39150.1; -.
DR   PaxDb; Q9FIC6; -.
DR   EnsemblPlants; AT5G39150.1; AT5G39150.1; AT5G39150.
DR   GeneID; 833908; -.
DR   Gramene; AT5G39150.1; AT5G39150.1; AT5G39150.
DR   KEGG; ath:AT5G39150; -.
DR   Araport; AT5G39150; -.
DR   TAIR; locus:2177187; AT5G39150.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_0_1; -.
DR   InParanoid; Q9FIC6; -.
DR   OMA; ATHMACA; -.
DR   OrthoDB; 1164277at2759; -.
DR   PhylomeDB; Q9FIC6; -.
DR   PRO; PR:Q9FIC6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIC6; baseline and differential.
DR   Genevisible; Q9FIC6; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   2: Evidence at transcript level;
KW   Apoplast; Disulfide bond; Glycoprotein; Manganese; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..221
FT                   /note="Germin-like protein subfamily 1 member 17"
FT                   /id="PRO_0000010817"
FT   DOMAIN          76..213
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..48
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  23733 MW;  6717B70BF102E673 CRC64;
     MKVSMSLILI TLSALVTIAK AYDPSPLQDF CVAIDDPKNG VFVNGKFCKD PKQAKAEDFF
     SSGLNQAGIT NNKVQSNVTT VNVDQIPGLN TLGISLVRID YAPYGQNPPH THPRATEILV
     LVEGTLYVGF VSSNQDNNRL FAKVLNPGDV FVFPIGMIHF QVNIGKTPAV AFAGLSSQNA
     GVITIADTVF GSTPPINPDI LAQAFQLDVN VVKDLEAKFK N